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- PDB-1ojd: HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH Lauryldimethylamine-N-o... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ojd | ||||||
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Title | HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH Lauryldimethylamine-N-oxide (LDAO) | ||||||
![]() | AMINE OXIDASE [FLAVIN-CONTAINING] B | ||||||
![]() | OXIDOREDUCTASE / FAD-CONTAINING AMINE OXIDASE / MAOB | ||||||
Function / homology | ![]() Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB / monoamine oxidase activity / monoamine oxidase / phenylethylamine catabolic process / positive regulation of dopamine metabolic process / response to aluminum ion / negative regulation of serotonin secretion / response to selenium ion / primary-amine oxidase / dopamine catabolic process ...Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB / monoamine oxidase activity / monoamine oxidase / phenylethylamine catabolic process / positive regulation of dopamine metabolic process / response to aluminum ion / negative regulation of serotonin secretion / response to selenium ion / primary-amine oxidase / dopamine catabolic process / aliphatic amine oxidase activity / primary methylamine oxidase activity / mitochondrial envelope / hydrogen peroxide biosynthetic process / response to corticosterone / substantia nigra development / response to toxic substance / flavin adenine dinucleotide binding / response to ethanol / mitochondrial outer membrane / response to lipopolysaccharide / electron transfer activity / response to xenobiotic stimulus / neuronal cell body / dendrite / mitochondrion / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Binda, C. / Edmondson, D.E. / Mattevi, A. | ||||||
![]() | ![]() Title: Insights Into the Mode of Inhibition of Human Mitochondrial Monoamine Oxidase B from High-Resolution Crystal Structures Authors: Binda, C. / Li, M. / Hubalek, F. / Restelli, N. / Edmondson, D.E. / Mattevi, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 958.6 KB | Display | ![]() |
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PDB format | ![]() | 796.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.8 MB | Display | ![]() |
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Full document | ![]() | 2.9 MB | Display | |
Data in XML | ![]() | 109.5 KB | Display | |
Data in CIF | ![]() | 154.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1oj9C ![]() 1ojaC ![]() 1ojcC ![]() 1gosS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 58837.730 Da / Num. of mol.: 10 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | ChemComp-FAD / #3: Chemical | ChemComp-LDA / Compound details | FUNCTION: CATALYZES THE OXIDATIVE DEAMINATION OF AMINES CATALYTIC ACTIVITY: RCH2NH2 + H2O + O2 = ...FUNCTION: CATALYZES THE OXIDATIVE DEAMINATIO | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 57 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.50 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→40 Å / Num. obs: 140447 / % possible obs: 98.4 % / Redundancy: 3.8 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 3.9 |
Reflection shell | Resolution: 3.1→3.27 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.201 / Mean I/σ(I) obs: 3.3 / % possible all: 97.8 |
Reflection | *PLUS Highest resolution: 3.1 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.088 |
Reflection shell | *PLUS % possible obs: 97.8 % / Rmerge(I) obs: 0.201 |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1GOS Resolution: 3.1→40 Å / SU B: 20.461 / SU ML: 0.366 / Cross valid method: THROUGHOUT / ESU R Free: 0.443
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Displacement parameters | Biso mean: 40.203 Å2
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Refinement step | Cycle: LAST / Resolution: 3.1→40 Å
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Refinement | *PLUS Rfactor Rfree: 0.26 / Rfactor Rwork: 0.252 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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